
Abstract
The heavy and light chains of botulinum A toxin were separated by anion exchange chromatography. Their intracellular actions were studied using bovine adrenal chromaffin cells permeabilized with streptolysin O. Purified light chain inhibited the Ca2+-stimulated [3H]noradrenaline release with a half-maximal effect at about 1.8 nM. The inhibition was incomplete. Heavy chain up to 28 nM was neither effective by itself nor did it enhance the inhibitory effect of light chain. It is concluded that the light chain of botulinum A toxin contains the functional domain responsible for the inhibition of exocytosis.
Item Type: | Journal article |
---|---|
Keywords: | Botulinum A toxin, Chain, light, Chain, heavy, Chromaffin cell, permeabilized, Exocytosis |
Faculties: | Medicine |
Subjects: | 600 Technology > 610 Medicine and health |
URN: | urn:nbn:de:bvb:19-epub-7143-1 |
Item ID: | 7143 |
Date Deposited: | 05. Nov 2008, 11:24 |
Last Modified: | 04. Nov 2020, 12:49 |